(data stored in ACNUC7421 zone)

SWISSPROT: PYRE_PSEU2

ID   PYRE_PSEU2              Reviewed;         213 AA.
AC   Q4ZZY3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   08-MAY-2019, entry version 98.
DE   RecName: Full=Orotate phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01208};
DE            Short=OPRT {ECO:0000255|HAMAP-Rule:MF_01208};
DE            Short=OPRTase {ECO:0000255|HAMAP-Rule:MF_01208};
DE            EC=2.4.2.10 {ECO:0000255|HAMAP-Rule:MF_01208};
GN   Name=pyrE {ECO:0000255|HAMAP-Rule:MF_01208};
GN   OrderedLocusNames=Psyr_0216;
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a;
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae
RT   pv. syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
CC   -!- FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from
CC       5-phosphoribose 1-diphosphate to orotate, leading to the formation
CC       of orotidine monophosphate (OMP). {ECO:0000255|HAMAP-
CC       Rule:MF_01208}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-
CC         ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380,
CC         ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538,
CC         ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01208};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01208};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; UMP from orotate: step 1/2. {ECO:0000255|HAMAP-
CC       Rule:MF_01208}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01208}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. PyrE subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01208}.
DR   EMBL; CP000075; AAY35289.1; -; Genomic_DNA.
DR   RefSeq; WP_003403990.1; NC_007005.1.
DR   RefSeq; YP_233327.1; NC_007005.1.
DR   SMR; Q4ZZY3; -.
DR   STRING; 205918.Psyr_0216; -.
DR   EnsemblBacteria; AAY35289; AAY35289; Psyr_0216.
DR   GeneID; 3365692; -.
DR   KEGG; psb:Psyr_0216; -.
DR   PATRIC; fig|205918.7.peg.213; -.
DR   eggNOG; ENOG4107QP2; Bacteria.
DR   eggNOG; COG0461; LUCA.
DR   HOGENOM; HOG000037974; -.
DR   KO; K00762; -.
DR   OMA; MKAYQRQ; -.
DR   BioCyc; PSYR205918:G1G4J-217-MONOMER; -.
DR   UniPathway; UPA00070; UER00119.
DR   Proteomes; UP000000426; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   HAMAP; MF_01208; PyrE; 1.
DR   InterPro; IPR023031; OPRT.
DR   InterPro; IPR004467; Or_phspho_trans_dom.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; SSF53271; 1.
DR   TIGRFAMs; TIGR00336; pyrE; 1.
DR   PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4ZZY3.
DR   SWISS-2DPAGE; Q4ZZY3.
KW   Complete proteome; Glycosyltransferase; Magnesium;
KW   Pyrimidine biosynthesis; Transferase.
FT   CHAIN         1    213       Orotate phosphoribosyltransferase.
FT                                /FTId=PRO_1000066278.
FT   REGION       34     35       Orotate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01208}.
FT   REGION       72     73       5-phosphoribose 1-diphosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01208}.
FT   REGION      124    132       5-phosphoribose 1-diphosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01208}.
FT   BINDING      26     26       5-phosphoribose 1-diphosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01208}.
FT   BINDING      99     99       5-phosphoribose 1-diphosphate; shared
FT                                with dimeric partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_01208}.
FT   BINDING     100    100       5-phosphoribose 1-diphosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01208}.
FT   BINDING     103    103       5-phosphoribose 1-diphosphate; shared
FT                                with dimeric partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_01208}.
FT   BINDING     105    105       5-phosphoribose 1-diphosphate; shared
FT                                with dimeric partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_01208}.
FT   BINDING     128    128       Orotate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01208}.
FT   BINDING     156    156       Orotate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01208}.
SQ   SEQUENCE   213 AA;  23037 MW;  7DEAF71F434ABFFA CRC64;
     MQAYQRDFIR FAIDRGVLRF GEFTLKSGRT SPYFFNAGLF NTGSALAQLG RFYAAAVVES
     GIAFDVLFGP AYKGIPLASA TAVALAEHHD RDLPWCFNRK EAKAHGEGGS LVGSPLAGNV
     LIIDDVITAG TAIREVMQII KDQDATAAGV LIALNRQERG NGELSAIQEV ERDFGIPVVS
     IVSLNQVLEF LADDPQLKQH LPAVEAYRAQ FGI
//

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